ArticleApplied and environmental microbiology2015
The N-Terminal GH10 Domain of a Multimodular Protein from Caldicellulosiruptor bescii Is a Versatile Xylanase/β-Glucanase That Can Degrade Crystalline Cellulose.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 57 citations in OpenAlex.
- Discovery and engineering of bifunctional enzymes for lignocellulose degradation: Metagenomic and computational approaches.Biotechnology reports (Amsterdam, Netherlands) · 2025Review
- Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse.Applied microbiology and biotechnology · 2025Article
- Effective Degradation of Brewer Spent Grains by a Novel Thermostable GH10 Xylanase.Applied biochemistry and biotechnology · 2024Article
- Characterization of a novel bifunctional enzyme from buffalo rumen metagenome and its effect on in vitro ruminal fermentation and microbial community composition.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2023Article
- Cloning, expression, and molecular modification of glycoside hydrolase family 5 genes from Thermoascus aurantiacus.PloS one · 2023Article
- Cellulose metabolism in halo(natrono)archaea: a comparative genomics study.Frontiers in microbiology · 2023Article
- Biochemical and Regulatory Analyses of Xylanolytic Regulons in Caldicellulosiruptor bescii Reveal Genus-Wide Features of Hemicellulose Utilization.Applied and environmental microbiology · 2022Article
- The Emergence of New Catalytic Abilities in an Endoxylanase from Family GH10 by Removing an Intrinsically Disordered Region.International journal of molecular sciences · 2022Article
- Multifunctional alkalophilic α-amylase with diverse raw seaweed degrading activities.AMB Express · 2021Article
- Rapid adaptation for fibre degradation by changes in plasmid stoichiometry within Lactobacillus plantarum at the synthetic community level.Microbial biotechnology · 2020Article
- Caldicellulosiruptor bescii Adheres to Polysaccharides via a Type IV Pilin-Dependent Mechanism.Applied and environmental microbiology · 2020Article
- Neotropical termite microbiomes as sources of novel plant cell wall degrading enzymes.Scientific reports · 2020Article
- The biology and biotechnology of the genus Caldicellulosiruptor: recent developments in 'Caldi World'.Extremophiles : life under extreme conditions · 2020Review
- Genomic and physiological analyses reveal that extremely thermophilic Caldicellulosiruptor changbaiensis deploys uncommon cellulose attachment mechanisms.Journal of industrial microbiology & biotechnology · 2019Article
- A Novel Subfamily of Endo-β-1,4-Glucanases in Glycoside Hydrolase Family 10.Applied and environmental microbiology · 2019Article
- Discovery of a Thermostable GH10 Xylanase with Broad Substrate Specificity from the Arctic Mid-Ocean Ridge Vent System.Applied and environmental microbiology · 2019Article
- Comparative Biochemical and Structural Analysis of Novel Cellulose Binding Proteins (Tāpirins) from Extremely ThermophilicApplied and environmental microbiology · 2019Article
- The GH10 and GH48 dual-functional catalytic domains from a multimodular glycoside hydrolase synergize in hydrolyzing both cellulose and xylan.Biotechnology for biofuels · 2019Article
- A novel thermostable GH10 xylanase with activities on a wide variety of cellulosic substrates from a xylanolyticBiotechnology for biofuels · 2019Article
- Improvement in catalytic activity and thermostability of a GH10 xylanase and its synergistic degradation of biomass with cellulase.Biotechnology for biofuels · 2019Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genome of the thermophilic bacterium Caldicellulosiruptor bescii encodes three multimodular enzymes with identical C-terminal domain organizations containing two consecutive CBM3b modules and one glycoside hydrolase (GH) family 48 (GH48) catalytic module. However, the three proteins differ much in their N termini. Among these proteins, CelA (or C. bescii Cel9A [CbCel9A]/Cel48A) with a GH9/CBM3c binary partner in the N terminus has been shown to use a novel strategy to degrade crystalline cellulose, which leads to its outstanding cellulose-cleaving activity. Here we show that C. bescii Xyn10C (CbXyn10C), the N-terminal GH10 domain from CbXyn10C/Cel48B, can also degrade crystalline cellulose, in addition to heterogeneous xylans and barley β-glucan. The data from substrate competition assays, mutational studies, molecular modeling, and docking point analyses point to the existence of only one catalytic center in the bifunctional xylanase/β-glucanase. The specific activities of the recombinant CbXyn10C on Avicel and filter paper were comparable to those of GH9/CBM3c of the robust CelA expressed in Escherichia coli. Appending one or two cellulose-binding CBM3bs enhanced the activities of CbXyn10C in degrading crystalline celluloses, which were again comparable to those of the GH9/CBM3c-CBM3b-CBM3b truncation mutant of CelA. Since CbXyn10C/Cel48B and CelA have similar domain organizations and high sequence homology, the endocellulase activity observed in CbXyn10C leads us to speculate that CbXyn10C/Cel48B may use the same strategy that CelA uses to hydrolyze crystalline cellulose, thus helping the excellent crystalline cellulose degrader C. bescii acquire energy from the environment. In addition, we also demonstrate that CbXyn10C may be an interesting candidate enzyme for biotechnology due to its versatility in hydrolyzing multiple substrates with different glycosidic linkages.
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